Institute of Molecular Physical Science, ETH Zürich, 8093 Zürich, Switzerland.
Institute of Technical and Macromolecular Chemistry, RWTH Aachen University, 52074 Aachen, Germany.
J Am Chem Soc. 2023 Oct 11;145(40):21915-21924. doi: 10.1021/jacs.3c06287. Epub 2023 Oct 2.
Interactions between RNA and proteins are the cornerstone of many important biological processes from transcription and translation to gene regulation, yet little is known about the ancient origin of said interactions. We hypothesized that peptide amyloids played a role in the origin of life and that their repetitive structure lends itself to building interfaces with other polymers through avidity. Here, we report that short RNA with a minimum length of three nucleotides binds in a sequence-dependent manner to peptide amyloids. The 3'-5' linked RNA backbone appears to be well-suited to support these interactions, with the phosphodiester backbone and nucleobases both contributing to the affinity. Sequence-specific RNA-peptide interactions of the kind identified here may provide a path to understanding one of the great mysteries rooted in the origin of life: the origin of the genetic code.
RNA 和蛋白质之间的相互作用是许多重要生物学过程的基础，包括转录和翻译以及基因调控，但人们对这些相互作用的古老起源知之甚少。我们假设肽淀粉样蛋白在生命起源中发挥了作用，并且其重复结构有助于通过亲和性与其他聚合物构建界面。在这里，我们报告了具有至少三个核苷酸长度的短 RNA 以序列依赖性方式与肽淀粉样蛋白结合。3'-5'连接的 RNA 骨架似乎非常适合支持这些相互作用，磷酸二酯骨架和核苷碱基都有助于亲和力。这里鉴定的这种序列特异性 RNA-肽相互作用可能为理解生命起源中一个伟大谜团之一提供了一条途径：遗传密码的起源。
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